PALMD_HUMAN
ID PALMD_HUMAN Reviewed; 551 AA.
AC Q9NP74; Q9H7E6; Q9NPM5; Q9NPM6; Q9NPS0;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Palmdelphin;
DE AltName: Full=Paralemmin-like protein;
GN Name=PALMD; Synonyms=C1orf11, PALML;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
RX PubMed=11478809; DOI=10.1006/bbrc.2001.5329;
RA Hu B., Copeland N.G., Gilbert D.J., Jenkins N.A., Kilimann M.W.;
RT "The paralemmin protein family: identification of paralemmin-2, an isoform
RT differentially spliced to AKAP2/AKAP-KL, and of palmdelphin, a more distant
RT cytosolic relative.";
RL Biochem. Biophys. Res. Commun. 285:1369-1376(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=11707320; DOI=10.1016/s0378-1119(01)00719-3;
RA Andreu N., Escarceller M., Feather S., Devriendt K., Wolf A.S.,
RA Estivill X., Sumoy L.;
RT "PALML, a novel paralemmin-related gene mapping on human chromosome 1p21.";
RL Gene 278:33-40(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RG The European IMAGE consortium;
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321 AND SER-520, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384 AND SER-498, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-179, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-125 AND LYS-179, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- SUBUNIT: Interacts with GLUL. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9NP74; O94929-2: ABLIM3; NbExp=3; IntAct=EBI-2811699, EBI-11961672;
CC Q9NP74; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-2811699, EBI-21603100;
CC Q9NP74; P42858: HTT; NbExp=6; IntAct=EBI-2811699, EBI-466029;
CC Q9NP74; O76024: WFS1; NbExp=3; IntAct=EBI-2811699, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11707320}. Cell
CC projection, dendrite {ECO:0000269|PubMed:11707320}. Cell projection,
CC dendritic spine {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NP74-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NP74-2; Sequence=VSP_021787;
CC Name=3;
CC IsoId=Q9NP74-3; Sequence=VSP_021786;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Most abundant in cardiac and skeletal
CC muscle. {ECO:0000269|PubMed:11707320}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the paralemmin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC01336.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AJ312214; CAC59692.1; -; mRNA.
DR EMBL; AF262379; AAL33879.1; -; mRNA.
DR EMBL; AK000278; BAA91047.1; -; mRNA.
DR EMBL; AK024654; BAB14946.1; -; mRNA.
DR EMBL; AL390970; CAC01335.1; -; mRNA.
DR EMBL; AL390971; CAC01336.1; ALT_SEQ; mRNA.
DR EMBL; AL390972; CAC01337.1; -; mRNA.
DR EMBL; AL390973; CAC01338.1; -; mRNA.
DR EMBL; BC012570; AAH12570.1; -; mRNA.
DR CCDS; CCDS758.1; -. [Q9NP74-1]
DR RefSeq; NP_060204.1; NM_017734.4. [Q9NP74-1]
DR AlphaFoldDB; Q9NP74; -.
DR SMR; Q9NP74; -.
DR BioGRID; 120221; 15.
DR IntAct; Q9NP74; 18.
DR STRING; 9606.ENSP00000263174; -.
DR iPTMnet; Q9NP74; -.
DR PhosphoSitePlus; Q9NP74; -.
DR BioMuta; PALMD; -.
DR DMDM; 74734298; -.
DR EPD; Q9NP74; -.
DR jPOST; Q9NP74; -.
DR MassIVE; Q9NP74; -.
DR MaxQB; Q9NP74; -.
DR PaxDb; Q9NP74; -.
DR PeptideAtlas; Q9NP74; -.
DR PRIDE; Q9NP74; -.
DR ProteomicsDB; 81912; -. [Q9NP74-1]
DR ProteomicsDB; 81913; -. [Q9NP74-2]
DR ProteomicsDB; 81914; -. [Q9NP74-3]
DR Antibodypedia; 2825; 150 antibodies from 26 providers.
DR DNASU; 54873; -.
DR Ensembl; ENST00000263174.9; ENSP00000263174.4; ENSG00000099260.12. [Q9NP74-1]
DR GeneID; 54873; -.
DR KEGG; hsa:54873; -.
DR MANE-Select; ENST00000263174.9; ENSP00000263174.4; NM_017734.5; NP_060204.1.
DR UCSC; uc001dsg.4; human. [Q9NP74-1]
DR CTD; 54873; -.
DR DisGeNET; 54873; -.
DR GeneCards; PALMD; -.
DR HGNC; HGNC:15846; PALMD.
DR HPA; ENSG00000099260; Tissue enhanced (adipose).
DR MIM; 610182; gene.
DR neXtProt; NX_Q9NP74; -.
DR OpenTargets; ENSG00000099260; -.
DR PharmGKB; PA32925; -.
DR VEuPathDB; HostDB:ENSG00000099260; -.
DR eggNOG; ENOG502QVMH; Eukaryota.
DR GeneTree; ENSGT00940000157718; -.
DR HOGENOM; CLU_038333_0_0_1; -.
DR InParanoid; Q9NP74; -.
DR PhylomeDB; Q9NP74; -.
DR TreeFam; TF105402; -.
DR PathwayCommons; Q9NP74; -.
DR SignaLink; Q9NP74; -.
DR BioGRID-ORCS; 54873; 9 hits in 1072 CRISPR screens.
DR ChiTaRS; PALMD; human.
DR GenomeRNAi; 54873; -.
DR Pharos; Q9NP74; Tbio.
DR PRO; PR:Q9NP74; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NP74; protein.
DR Bgee; ENSG00000099260; Expressed in synovial joint and 185 other tissues.
DR ExpressionAtlas; Q9NP74; baseline and differential.
DR Genevisible; Q9NP74; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:InterPro.
DR InterPro; IPR004965; Paralemmin.
DR Pfam; PF03285; Paralemmin; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Synapse;
KW Ubl conjugation.
FT CHAIN 1..551
FT /note="Palmdelphin"
FT /id="PRO_0000262528"
FT REGION 248..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 12..106
FT /evidence="ECO:0000255"
FT COMPBIAS 484..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 271
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHU2"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHU2"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHU2"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 125
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..175
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021786"
FT VAR_SEQ 1..99
FT /note="MEEAELVKGRLQAITDKRKIQEEISQKRLKIEEDKLKHQHLKKKALREKWLL
FT DGISSGKEQEEMKKQNQQDQHQIQVLEQSILRLEKEIQDLEKAELQI -> MASRWNQQ
FT RKRTGRDEEAK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11707320, ECO:0000303|Ref.4"
FT /id="VSP_021787"
FT VARIANT 73
FT /note="H -> Q (in dbSNP:rs11802902)"
FT /id="VAR_053805"
FT VARIANT 229
FT /note="N -> S (in dbSNP:rs35258980)"
FT /id="VAR_053806"
FT VARIANT 459
FT /note="E -> D (in dbSNP:rs35317701)"
FT /id="VAR_053807"
FT CONFLICT 248
FT /note="E -> K (in Ref. 3; BAB14946)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="S -> L (in Ref. 4; CAC01335)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 551 AA; 62758 MW; CC93EAC5ED5625D7 CRC64;
MEEAELVKGR LQAITDKRKI QEEISQKRLK IEEDKLKHQH LKKKALREKW LLDGISSGKE
QEEMKKQNQQ DQHQIQVLEQ SILRLEKEIQ DLEKAELQIS TKEEAILKKL KSIERTTEDI
IRSVKVEREE RAEESIEDIY ANIPDLPKSY IPSRLRKEIN EEKEDDEQNR KALYAMEIKV
EKDLKTGEST VLSSIPLPSD DFKGTGIKVY DDGQKSVYAV SSNHSAAYNG TDGLAPVEVE
ELLRQASERN SKSPTEYHEP VYANPFYRPT TPQRETVTPG PNFQERIKIK TNGLGIGVNE
SIHNMGNGLS EERGNNFNHI SPIPPVPHPR SVIQQAEEKL HTPQKRLMTP WEESNVMQDK
DAPSPKPRLS PRETIFGKSE HQNSSPTCQE DEEDVRYNIV HSLPPDINDT EPVTMIFMGY
QQAEDSEEDK KFLTGYDGII HAELVVIDDE EEEDEGEAEK PSYHPIAPHS QVYQPAKPTP
LPRKRSEASP HENTNHKSPH KNSISLKEQE ESLGSPVHHS PFDAQTTGDG TEDPSLTALR
MRMAKLGKKV I
